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P14488

- BLAB_BACCE

UniProt

P14488 - BLAB_BACCE

Protein

Beta-lactamase 2

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Can hydrolyze carbapenem compounds.

    Catalytic activityi

    A beta-lactam + H2O = a substituted beta-amino acid.

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi115 – 1151Zinc 1By similarity
    Metal bindingi117 – 1171Zinc 1By similarity
    Metal bindingi119 – 1191Zinc 2By similarity
    Metal bindingi178 – 1781Zinc 1By similarity
    Metal bindingi197 – 1971Zinc 2By similarity
    Metal bindingi239 – 2391Zinc 2By similarity

    GO - Molecular functioni

    1. beta-lactamase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. antibiotic catabolic process Source: InterPro
    2. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP14488.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase 2 (EC:3.5.2.6)
    Alternative name(s):
    Beta-lactamase II
    Cephalosporinase
    Penicillinase
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi110 – 1101D → N: No change in activity.
    Mutagenesisi119 – 1191D → N or E: Inactivates the enzyme.
    Mutagenesisi177 – 1771G → E: Inactivates the enzyme.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Add
    BLAST
    Chaini30 – 256227Beta-lactamase 2PRO_0000016943Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP14488.
    SMRiP14488. Positions 37-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Beta-lactamas-like.
    IPR001018. Beta-lactamase_class-B_CS.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.
    PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
    PS00744. BETA_LACTAMASE_B_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14488-1 [UniParc]FASTAAdd to Basket

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    MKNTLLKLGV CVSLLGITPF VSTISSVQAE RTVEHKVIKN ETGTISISQL    50
    NKNVWVHTEL GYFSGEAVPS NGLVLNTSKG LVLVDSSWDD KLTKELIEMV 100
    EKKFKKRVTD VIITHAHADR IGGMKTLKER GIKAHSTALT AELAKKNGYE 150
    EPLGDLQSVT NLKFGNMKVE TFYPGKGHTE DNIVVWLPQY QILAGGCLVK 200
    SASSKDLGNV ADAYVNEWST SIENVLKRYG NINLVVPGHG EVGDRGLLLH 250
    TLDLLK 256
    Length:256
    Mass (Da):28,038
    Last modified:January 1, 1990 - v1
    Checksum:i670F62378C355C2D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19530 Genomic DNA. Translation: AAA22562.1.
    PIRiA32017.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19530 Genomic DNA. Translation: AAA22562.1 .
    PIRi A32017.

    3D structure databases

    ProteinModelPortali P14488.
    SMRi P14488. Positions 37-246.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1744488.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P14488.

    Family and domain databases

    Gene3Di 3.60.15.10. 1 hit.
    InterProi IPR001279. Beta-lactamas-like.
    IPR001018. Beta-lactamase_class-B_CS.
    [Graphical view ]
    Pfami PF00753. Lactamase_B. 1 hit.
    [Graphical view ]
    SMARTi SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56281. SSF56281. 1 hit.
    PROSITEi PS00743. BETA_LACTAMASE_B_1. 1 hit.
    PS00744. BETA_LACTAMASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene."
      Lim H.M., Pene J.J., Shaw R.W.
      J. Bacteriol. 170:2873-2878(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 5/B/6.
    2. "Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II."
      Lim H.M., Pene J.J.
      J. Biol. Chem. 264:11682-11687(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    3. "Site-directed mutagenesis of dicarboxylic acids near the active site of Bacillus cereus 5/B/6 beta-lactamase II."
      Lim H.M., Iyer R.K., Pene J.J.
      Biochem. J. 276:401-404(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.

    Entry informationi

    Entry nameiBLAB_BACCE
    AccessioniPrimary (citable) accession number: P14488
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3